Interaction of monomeric and dimeric kinesin with microtubules.
The binding stoichiometry of kinesin to microtubules was determined using several biochemical and biophysical approaches (chemical crosslinking, binding assays, scanning transmission electron microscopy (STEM), image reconstruction, and X-ray scattering). The results show that each tubulin dimer associates with one kinesin head, irrespective of whether kinesin occurs in a monomeric or dimeric form in solution. Moreover, these heads appear to align along the protofilament axis generating a 16 nm periodicity of successive kinesin dimers. This is consistent with a "tightrope" model of movement where the first head of the dimer provides a guiding signal for the following one.
Thormählen
M
M
Max-Planck-Unit for Structural Molecular Biology, Notkestrasse 85, Hamburg, D-22603, Germany.
Marx
A
A
Müller
S A
SA
Song
Y
Y
Mandelkow
E M
EM
Aebi
U
U
Mandelkow
E
E
D000818:Animals; D001665:Binding Sites; D049832:Decapodiformes; D016547:Kinesins / Q000737:chemistry / Q000378:metabolism*; D008855:Microscopy, Electron, Scanning; D008870:Microtubules / Q000737:chemistry / Q000378:metabolism* / Q000648:ultrastructure; D011487:Protein Conformation; D051381:Rats; D014404:Tubulin / Q000737:chemistry / Q000378:metabolism*; D014961:X-Ray Diffraction
D014404:Tubulin; D016547:Kinesins